Association of Increased Receptor-Binding Avidity of Influenza A(H9N2) Viruses with Escape from Antibody-Based Immunity and Enhanced Zoonotic Potential
Joshua E. Sealy, Tahir Yaqub, Thomas P. Peacock1
, Pengxiang Chang, Burcu Ermetal, Anabel Clements, Jean-Remy Sadeyen, Arslan Mehboob2
, Holly Shelton, Juliet E. Bryant, Rod S. Daniels, John W. McCauley, Munir Iqbal
, and Jean-Remy Royal Veterinary CollegeLondonUKSadeyen
Author affiliations: The Pirbright Institute, Pirbright, UK (J.E. Sealy, T.P. Peacock, P. Chang, A. Clements, J.-R. Sadeyen, H. Shelton, M. Iqbal); University of Veterinary and Animal Sciences, Lahore, Pakistan (T. Yaqub, A. Mehboob); The Francis Crick Institute, London (B. Ermetal, R.S. Daniels, J.W. McCauley); Fondation Mérieux, Lyon, France (J.E. Bryant)
Figure 4. Receptor-binding profiles of influenza A(H9N2) virus isolates from Pakistan with HA residue 180 substitutions. A, B) UDL-01/08 viruses containing A180T/V substitutions: A) H9N2 A/chicken/Pakistan/UDL-10/2008 A180T; B) H9N2 A/chicken/Pakistan/UDL-10/2008 A180V. C, D) SKP-827/16 viruses containing T180A/V substitutions: C) H9N2 A/chicken/Pakistan/SKP-227/2016 T180A; D) H9N2 A/chicken/Pakistan/SKP-227/2016 T180V. Dashed lines indicate binding profiles of wild-type viruses UDL-01/08 with A180 and SKP-827/16 with T180, and solid lines indicate binding profiles of variant viruses. HA, hemagglutinin.
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